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Conserved domains on  [gi|1622956763|ref|XP_028707613|]
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ankyrin repeat and SOCS box protein 2 isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-400 6.73e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 6.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 125 IKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKS 204
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 205 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQL 284
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 285 EALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-T 363
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlN 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622956763 364 RVRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPLA 400
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
591-635 1.14e-23

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


:

Pssm-ID: 239691  Cd Length: 45  Bit Score: 93.78  E-value: 1.14e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 635
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 9.15e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 373 LHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1622956763 451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-400 6.73e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 6.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 125 IKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKS 204
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 205 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQL 284
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 285 EALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-T 363
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlN 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622956763 364 RVRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPLA 400
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA02876 PHA02876
ankyrin repeat protein; Provisional
165-469 2.55e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 107.84  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 244
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 245 SVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDSASALYEACKNEHE-EVVEF 322
Cdd:PHA02876  247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 323 LLLQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRVRR-SGVSPLHLAAERNNDAVLEALLSARFDVNApla 400
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 401 perarlYEDRRSSALYFAVVNNNVY-ATELLLEHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 469
Cdd:PHA02876  404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
591-635 1.14e-23

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 93.78  E-value: 1.14e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 635
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-300 1.92e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 209 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNgGAKVESKNaYGITPLFVAAQSGQLEALR 288
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1622956763 289 FLAKYGADINTQ 300
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 9.15e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 373 LHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1622956763 451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
592-630 2.41e-11

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 58.72  E-value: 2.41e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956763 592 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 630
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
140-357 5.23e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 140 LPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 220 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLE 285
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 286 ALRFLAKYGADINTQASDSASALY----EACKNEHEEVVEFLLLQGADANK------TNKDGLLPLHIASKKGNYRIVQM 355
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230

                  ..
gi 1622956763 356 LL 357
Cdd:cd22192   231 LV 232
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
594-632 2.65e-08

The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases;


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.71  E-value: 2.65e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622956763  594 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 632
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
339-486 6.77e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 339 LPLHIASKKGNYRIVQMLLpVTSRTRVRRSGV---SPLHLAAERNNDAVLEALL-SARFDVNAPLAPErarLYEDRrsSA 414
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 415 LYFAVVNNNVYATELLLEHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 1622956763 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
237-357 8.07e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622956763 303 DS-----ASALYEACKNEHEEVV----EFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02884 PHA02884
ankyrin repeat protein; Provisional
384-503 2.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 384 VLEALLSARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLEHGADPNR----DVISPLLVAIRHGCLRTMQL 459
Cdd:PHA02884   48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622956763 460 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884  123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
270-298 1.75e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.75e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622956763  270 YGITPLFVAAQSGQLEALRFLAKYGADIN 298
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
443-469 8.66e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.66e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622956763  443 SPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
125-400 6.73e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 6.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 125 IKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKS 204
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 205 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQL 284
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 285 EALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-T 363
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlN 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622956763 364 RVRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPLA 400
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
109-357 2.69e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 2.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 109 LIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCL 188
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 189 LSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKN 268
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 269 AYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKG 348
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                  ....*....
gi 1622956763 349 NYRIVQMLL 357
Cdd:COG0666   264 AALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
107-341 6.02e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 6.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 107 DPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAyPGTIDQRTLQEETAVYLATCRGHLD 186
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 187 CLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVES 266
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956763 267 KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPL 341
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
188-478 2.60e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 2.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESK 267
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 268 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKK 347
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 348 GNYRIVQMLL----PVTSRTrvrRSGVSPLHLAAERNNDAVLEALLSARFDVNAPlaperarlyEDRRSSALYFAVVNNN 423
Cdd:COG0666   164 GNLEIVKLLLeagaDVNARD---NDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGN 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622956763 424 VYATELLLEHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAF 478
Cdd:COG0666   232 LEIVKLLLEAGADLNakdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
218-477 1.47e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 218 AEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI 297
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 298 NTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrvrRSGVSPL 373
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeagaDVNAQD---NDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 374 HLAAERNNDAVLEALLSARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLEHGADPN---RDVISPLLVAIR 450
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIVKLLLEAGADVNakdNDGKTALDLAAE 228
                         250       260
                  ....*....|....*....|....*..
gi 1622956763 451 HGCLRTMQLLLDHGANIDAYIATHPTA 477
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
165-469 2.55e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 107.84  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 244
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 245 SVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDSASALYEACKNEHE-EVVEF 322
Cdd:PHA02876  247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 323 LLLQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRVRR-SGVSPLHLAAERNNDAVLEALLSARFDVNApla 400
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 401 perarlYEDRRSSALYFAVVNNNVY-ATELLLEHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 469
Cdd:PHA02876  404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
198-397 3.15e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.52  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 198 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMEILVNGGAKVESKNAYGI 272
Cdd:PHA03100   28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 273 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDSASALYEACKNEHE--EVVEFLLLQGADANKTNK-DGLL-------- 339
Cdd:PHA03100  108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622956763 340 -------PLHIASKKGNYRIVQMLLPVTSRTRVR-RSGVSPLHLAAERNNDAVLEALLSARFDVNA 397
Cdd:PHA03100  188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
591-635 1.14e-23

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 93.78  E-value: 1.14e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 635
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03095 PHA03095
ankyrin-like protein; Provisional
199-480 6.25e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.41  E-value: 6.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 199 DISNKSRETPLYK---ACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMEILVNGGAKVESKNAYGI 272
Cdd:PHA03095    5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 273 TPLFVAAQSGQ-LEALRFLAKYGADINTQ--ASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHI--ASKK 347
Cdd:PHA03095   85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 348 GNYRIVQMLLPVTSRTRVRRS-GVSPLHLAAE--RNNDAVLEALLSARFDVNAPLAPERARLYED------RRS------ 412
Cdd:PHA03095  165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgsscKRSlvlpll 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 413 --------------SALYFAVVNNNVYATELLLEHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 475
Cdd:PHA03095  245 iagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324

                  ....*
gi 1622956763 476 TAFPA 480
Cdd:PHA03095  325 TASVA 329
PHA03100 PHA03100
ankyrin repeat protein; Provisional
177-357 2.01e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.04  E-value: 2.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 177 YLATCRGHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR--N 249
Cdd:PHA03100   40 YLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 250 DLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQ--LEALRFLAKYGADINtqASDSA------------------SALY 309
Cdd:PHA03100  120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDIN--AKNRVnyllsygvpinikdvygfTPLH 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622956763 310 EACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-300 1.92e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 209 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNgGAKVESKNaYGITPLFVAAQSGQLEALR 288
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1622956763 289 FLAKYGADINTQ 300
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
106-406 6.41e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.64  E-value: 6.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 106 VDPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLqraypgtIDQRTlqeETAVYLATCRGHl 185
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL-------IDNGV---DTSILPIPCIEK- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 186 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVE 265
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 266 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKneHEEVVEFLLLQGADANKTNKDGLLPLHIA- 344
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAi 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 345 SKKGNYRIVQMLLPVTSRTRVR-RSGVSPLHLAAER-NNDAVLEALLSarfdvNAPLAPERARL 406
Cdd:PHA02874  263 NPPCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA-----NAVLIKEADKL 321
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-268 9.97e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 9.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 178 LATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHnADTNHRCNrGWTALHESVSRNDLEVMEIL 257
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80
                          90
                  ....*....|.
gi 1622956763 258 VNGGAKVESKN 268
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
199-384 1.07e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.87  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 199 DISNKSRETPLYKACERKNAEAVKILVQHNADTNHRC----NRGWTALheSVSRNDL---------------------EV 253
Cdd:PHA02874   29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAI--KIGAHDIikllidngvdtsilpipciekDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 254 MEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKT 333
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622956763 334 NKDGLLPLHIASKKGNYRIVQMLLPVTSRTRVR-RSGVSPLHLAAERNNDAV 384
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRSAI 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
308-397 1.86e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 308 LYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPvTSRTRVRRSGVSPLHLAAERNNDAVLEA 387
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|
gi 1622956763 388 LLSARFDVNA 397
Cdd:pfam12796  80 LLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
179-396 2.21e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 2.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 179 ATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILV 258
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 259 NGGAKVES---KNayGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNK 335
Cdd:PHA02875   89 DLGKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 336 DGLLPLHIASKKGNYRIVQMLLPVTSRTRV--RRSGVSPLHLAAERNNDAVLEALLSARFDVN 396
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-334 3.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 242 LHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYgADINTQASDSaSALYEACKNEHEEVVE 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1622956763 322 FLLLQGADANKTN 334
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
106-298 1.06e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.81  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 106 VDPLIKAIKNGDEEALKTMIKEGK--NLAEPNKEGwlPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRG 183
Cdd:PHA02875   36 ISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAK 263
Cdd:PHA02875  114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622956763 264 VE--SKNAyGITPLFVAAQSGQLEALRFLAKYGADIN 298
Cdd:PHA02875  194 IDyfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
184-463 1.47e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 85.70  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQhnadTNHRCNRGWT--ALHESVSRNDLEVME-ILVNg 260
Cdd:PHA02878   49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEIFKiILTN- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 261 gakvESKNAYGITPLFVAAQSG----QLEALRFLAKYGADINTQASDS-ASALYEACKNEHEEVVEFLLLQGADANKTNK 335
Cdd:PHA02878  124 ----RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 336 DGLLPLHIASKKGNYRIVQMLLPVTSRTRVRRS-GVSPLHLAAERNND-AVLEALLSARFDVNAPLAPerarlyedRRSS 413
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYI--------LGLT 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 414 ALYFAVVNNNVyaTELLLEHGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 463
Cdd:PHA02878  272 ALHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
275-357 1.52e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 275 LFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEfLLLQGADANKTNkDGLLPLHIASKKGNYRIVQ 354
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ...
gi 1622956763 355 MLL 357
Cdd:pfam12796  79 LLL 81
PHA02876 PHA02876
ankyrin repeat protein; Provisional
109-367 5.99e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.73  E-value: 5.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 109 LIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCL--KVLQRAypGTIDQRTLQEETAVYLATCRGH-L 185
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLMAKNGYdT 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 186 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKV 264
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 265 ES-KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHE-EVVEFLLLQGADANKTNKDGLLPLH 342
Cdd:PHA02876  402 EAlSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481
                         250       260
                  ....*....|....*....|....*
gi 1622956763 343 IAskKGNYRIVQMLLPVTSRTRVRR 367
Cdd:PHA02876  482 IA--LEYHGIVNILLHYGAELRDSR 504
PHA03100 PHA03100
ankyrin repeat protein; Provisional
244-473 7.98e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 7.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 244 ESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEH-----EE 318
Cdd:PHA03100    8 TKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 319 VVEFLLLQGADANKTNKDGLLPLHIAS--KKGNYRIVQMLLPVTSRTRVRRS-GVSPLHLAAERNND--AVLEALLSARF 393
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 394 DVNA------------PLaperarLYEDRR-SSALYFAVVNNNVYATELLLEHGADPN-RDVI--SPLLVAIRHGCLRTM 457
Cdd:PHA03100  168 DINAknrvnyllsygvPI------NIKDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIF 241
                         250
                  ....*....|....*.
gi 1622956763 458 QLLLDHGANIDAYIAT 473
Cdd:PHA03100  242 KLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
174-313 9.86e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 9.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 174 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR-NDLE 252
Cdd:PHA02878  170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622956763 253 VMEILVNGGAKVESKNA-YGITPLFVAAQSGQleALRFLAKYGADINTQASDSASALYEACK 313
Cdd:PHA02878  250 ILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
91-347 5.18e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.08  E-value: 5.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763  91 QKYSSSLfqtsQLAPVDPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLH--------------------------- 143
Cdd:PHA02878   27 ENYSTSA----SLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytl 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 144 ----EAAYYGQLGCLK-VLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLslLQAGAEPDISNKSR-ETPLYKACERKN 217
Cdd:PHA02878  103 vaikDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLL--LSYGADINMKDRHKgNTALHYATENKD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 218 AEAVKILVQHNADTN--HRCNRgwTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQS-GQLEALRFLAKYG 294
Cdd:PHA02878  181 QRLTELLLSYGANVNipDKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 295 ADINTQAS-DSASALYEACKNEheEVVEFLLLQGADANKTNKDGLLPLHIASKK 347
Cdd:PHA02878  259 VDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
242-501 7.99e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 7.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 242 LHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASA-------------- 307
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlecavdsknidtik 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 308 ------------------------------LYEA---------CKNE--HEEV--------VEFLLLQGADANKTNKDGL 338
Cdd:PHA02876  229 aiidnrsninkndlsllkairnedletsllLYDAgfsvnsiddCKNTplHHASqapslsrlVPKLLERGADVNAKNIKGE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 339 LPLHIASKKG----NYRIVQMLLPVTSRTrvRRSGVSPLHLAA--ERNNDAVLeALLSARFDVNaplaperARLYEDRrs 412
Cdd:PHA02876  309 TPLYLMAKNGydteNIRTLIMLGADVNAA--DRLYITPLHQAStlDRNKDIVI-TLLELGANVN-------ARDYCDK-- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 413 SALYFAVVNNNVYATELLLEHGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIM 483
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYA 449
                         330
                  ....*....|....*....
gi 1622956763 484 FAMKC-LSLLKFLMDLGCD 501
Cdd:PHA02876  450 CKKNCkLDVIEMLLDNGAD 468
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
188-336 8.22e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.99  E-value: 8.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGgAKVESK 267
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDP 619
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622956763 268 NAYGiTPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKD 336
Cdd:PLN03192  620 HAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
278-475 9.14e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 9.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 278 AAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 358 PVTSRTR--VRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLEHGA 435
Cdd:PHA02875   89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622956763 436 DPNRDV---ISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 475
Cdd:PHA02875  160 CLDIEDccgCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
117-358 1.30e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 117 DEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQ-LGCLKVLQRA-----YPGTIDQRTLQeetaVYLATCRGHLDCLLS 190
Cdd:PHA03095   62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNINPKVIRL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 191 LLQAGAEPDISNKSRETPLYKACERKNA--EAVKILVQHNADTNHRCNRGWTALH---ESVsRNDLEVMEILVNGGAKVE 265
Cdd:PHA03095  138 LLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlQSF-KPRARIVRELIRAGCDPA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 266 SKNAYGITPLFVAAQSGQLEALR---FLAKyGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLH 342
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRSLvlpLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295
                         250
                  ....*....|....*.
gi 1622956763 343 IASKKGNYRIVQMLLP 358
Cdd:PHA03095  296 LMVRNNNGRAVRAALA 311
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
591-632 5.14e-14

SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain.


Pssm-ID: 239686  Cd Length: 42  Bit Score: 66.37  E-value: 5.14e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
593-632 9.48e-14

SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239641  Cd Length: 41  Bit Score: 65.57  E-value: 9.48e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-202 8.32e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 8.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 109 LIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1622956763 189 LSLLQAGAEPDISN 202
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 9.15e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 373 LHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1622956763 451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
281-475 1.31e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 281 SGQLEALRFLAKYGAD-INTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPv 359
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 360 tsrtrvrrSGVSPLHLAAERNNDAVLEALLSARFDVNAplaperarlyEDRRSSA-LYFAVVNNNVYATELLLEHGADPN 438
Cdd:PHA02874   90 --------NGVDTSILPIPCIEKDMIKTILDCGIDVNI----------KDAELKTfLHYAIKKGDLESIKMLFEYGADVN 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622956763 439 RDVIS---PLLVAIRHGCLRTMQLLLDHGA--NIDAYIATHP 475
Cdd:PHA02874  152 IEDDNgcyPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESP 193
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
592-630 2.41e-11

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 58.72  E-value: 2.41e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956763 592 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 630
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
174-315 2.48e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 174 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCnrGWTALHESVSRNDLEV 253
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTA 637
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956763 254 MEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI---NTQASDSASALYEACKNE 315
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTELRELLQKR 702
Ank_4 pfam13637
Ankyrin repeats (many copies);
306-357 3.37e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 3.37e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622956763 306 SALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
202-348 3.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 62.91  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 202 NKSRETPLYKACERKNA--EAVKILVQHNADTNHRC-NRGWTALHESVSRN---DLEVMEILVNGGAKVESKNAYGITPL 275
Cdd:PHA02859   48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622956763 276 --FVAAQSGQLEALRFLAKYGADINTQASDSASALYEACK-NEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKG 348
Cdd:PHA02859  128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
273-324 2.96e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 2.96e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622956763 273 TPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLL 324
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
140-357 5.23e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 140 LPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 220 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLE 285
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 286 ALRFLAKYGADINTQASDSASALY----EACKNEHEEVVEFLLLQGADANK------TNKDGLLPLHIASKKGNYRIVQM 355
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230

                  ..
gi 1622956763 356 LL 357
Cdd:cd22192   231 LV 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
300-469 5.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 5.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 300 QASDSASA-----LYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRVRRSGVSpLH 374
Cdd:PHA02878   28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA-IK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 375 LAAERNNDAVLEALLSARFDVN--------------APLAPERARLY-----------EDRRSSALYFAVVNNNVYATEL 429
Cdd:PHA02878  107 DAFNNRNVEIFKIILTNRYKNIqtidlvyidkkskdDIIEAEITKLLlsygadinmkdRHKGNTALHYATENKDQRLTEL 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622956763 430 LLEHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:PHA02878  187 LLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
PHA02798 PHA02798
ankyrin-like protein; Provisional
221-450 1.57e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.62  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 221 VKILVQHNADTNHRCNRGWTALHESVSR---NDLEVMEILVNGGAKVESKNAYGITPLFVAAQSG---QLEALRFLAKYG 294
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 295 ADINTQAS----DSASALYEACKNEHE-EVVEFLLLQGADANKTNK-------DGLLPLHIASKKGNYRIVQMLLPVTSR 362
Cdd:PHA02798  172 VDINTHNNkekyDTLHCYFKYNIDRIDaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 363 TRVRRSGVSPLHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgaDPNRDVI 442
Cdd:PHA02798  252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN---------IITELGNTCLFTAFENESKFIFNSILNK--KPNKNTI 320

                  ....*...
gi 1622956763 443 SPLLVAIR 450
Cdd:PHA02798  321 SYTYYKLR 328
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
108-292 9.54e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.49  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 108 PLIKAIKNGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQE----ETAVYLATCR 182
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgETALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 183 GHLDCLLSLLQAGAepDISN---------KSR-------ETPL-YKACErKNAEAVKILVQHNADTNHRCNRGWTALHES 245
Cdd:cd22192   100 QNLNLVRELIARGA--DVVSpratgtffrPGPknliyygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622956763 246 VSRND----LEVMEILVNGGAKVES------KNAYGITPLFVAAQSGQLEALRFLAK 292
Cdd:cd22192   177 VLQPNktfaCQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
594-632 2.65e-08

The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases;


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.71  E-value: 2.65e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622956763  594 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 632
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
593-632 5.00e-08

SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 and SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF) and also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239688  Cd Length: 42  Bit Score: 49.22  E-value: 5.00e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
PHA02946 PHA02946
ankyin-like protein; Provisional
191-375 5.36e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.45  E-value: 5.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 191 LLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHeSVSRNDLEVME---ILVNGGAKVE-S 266
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKINnS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 267 KNAYGITPLFVAAQSGQLEALRFLA-KYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIAS 345
Cdd:PHA02946  137 VDEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622956763 346 KK--GNYRIVQMLLPVTSRTRVRRSGVSPLHL 375
Cdd:PHA02946  217 SKtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
279-357 6.40e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 6.40e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622956763 279 AQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
108-270 8.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 8.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 108 PLIKAI--KNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGcLKVLQraypgtidqrTLQEETAVYLATCRghL 185
Cdd:PHA03100  109 PLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILK----------LLIDKGVDINAKNR--V 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 186 DCLLSLlqaGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVE 265
Cdd:PHA03100  176 NYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                  ....*
gi 1622956763 266 SKNAY 270
Cdd:PHA03100  253 TIIET 257
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
593-632 1.06e-07

SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239690  Cd Length: 42  Bit Score: 48.57  E-value: 1.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03720     3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-258 1.24e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 205 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILV 258
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
591-632 1.40e-07

SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239700  Cd Length: 57  Bit Score: 48.69  E-value: 1.40e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 632
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
205-392 1.55e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 205 RETPLYKACERKNAEAVK-ILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAK-----VESKNAYGITPLFVA 278
Cdd:cd22192    17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 279 AQSGQLEALRFLAKYGADINTQA------SDSASAL---------YEACKNeHEEVVEFLLLQGADANKTNKDGLLPLHI 343
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygehplsFAACVG-NEEIVRLLIEHGADIRAQDSLGNTVLHI 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 344 ----ASKKGNYRIVQMLL-------PVTSRTRVRRSGVSPLHLAAERNNDAVLEALLSAR 392
Cdd:cd22192   176 lvlqPNKTFACQMYDLILsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-157 2.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622956763 107 DPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVL 157
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
593-631 3.09e-07

SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain.


Pssm-ID: 239687  Cd Length: 39  Bit Score: 46.82  E-value: 3.09e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 631
Cdd:cd03717     3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
593-632 3.30e-07

SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB4, like SSB2 and SSB1, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239712  Cd Length: 42  Bit Score: 46.87  E-value: 3.30e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
594-633 5.54e-07

SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS7 is important in the functioning of neuronal cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239710  Cd Length: 49  Bit Score: 46.63  E-value: 5.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 594 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 633
Cdd:cd03741     4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
339-486 6.77e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 339 LPLHIASKKGNYRIVQMLLpVTSRTRVRRSGV---SPLHLAAERNNDAVLEALL-SARFDVNAPLAPErarLYEDRrsSA 414
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 415 LYFAVVNNNVYATELLLEHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 1622956763 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
237-357 8.07e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622956763 303 DS-----ASALYEACKNEHEEVV----EFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
228-357 1.81e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.91  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 228 NADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKY 293
Cdd:cd22194   131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEK 210
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622956763 294 GADINTqASDSAS-----ALYEACKNEHE------EVVEFLLLQGADAN---KTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22194   211 ESTDIT-SQDSRGntvlhALVTVAEDSKTqndfvkRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
384-503 2.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 384 VLEALLSARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLEHGADPNR----DVISPLLVAIRHGCLRTMQL 459
Cdd:PHA02884   48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622956763 460 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884  123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
587-631 2.52e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.59  E-value: 2.52e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622956763  587 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 631
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-243 4.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 4.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 191 LLQAG-AEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
242-436 5.28e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 242 LHESVSRNDLEVMEILV-NGGAKVESKNAYGITPLFVAAQSGQLEALrFLAKYGADINTqaSDSASALYEACKNEHEEVV 320
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGdNGGEHDDPNMASNLLTVASTGNAALLEEL-LKAKLDPDIGD--SKGRTPLHIAASKGYEDCV 574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 321 EFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRVRRSGvSPLHLAAERNNDAVLEALLSARFDVNApla 400
Cdd:PLN03192  575 LVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS--- 650
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622956763 401 perarlyEDRR-SSALYFAVVNNNVYATELLLEHGAD 436
Cdd:PLN03192  651 -------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
237-357 6.03e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.49  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 302
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQ 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 303 DSAS-----ALYEACKNEHE------EVVEFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd21882   152 DSLGntvlhALVLQADNTPEnsafvcQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-290 6.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 6.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 238 GWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFL 290
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
591-632 7.57e-06

SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB2 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB2, like SSB4 and SSB1, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239689  Cd Length: 42  Bit Score: 43.09  E-value: 7.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03719     1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
593-632 9.66e-06

SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), both the absence and the presence of HGF and enhances the HGF-MET-induced mitogen-activated protein kinases Erk-transcription factor Elk-1-serum response elements (SRE) pathway. SSB1, like SSB2 and SSB4, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239713  Cd Length: 42  Bit Score: 43.05  E-value: 9.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
591-632 1.17e-05

SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB15 is expressed predominantly in skeletal muscle and participates in the regulation of protein turnover and muscle cell development by stimulating protein synthesis and regulating differentiation of muscle cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239701  Cd Length: 56  Bit Score: 42.90  E-value: 1.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956763 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 632
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-225 1.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622956763 182 RGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILV 225
Cdd:pfam13637  11 SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-157 2.38e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 2.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622956763 108 PLIKAIKNGDEEALKTMIKegKNLAEPNKEGWLPLHEAAYYGQLGCLKVL 157
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLL 80
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
237-357 2.87e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.10  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFL---AKYGADINT 299
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 300 QASDSAS---ALYEACKNEHEE------VVEFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22193   155 QDSRGNTvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
264-438 3.26e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 264 VESKNAYGITPLFVAAQSGQLEALRFLAKYgadINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTnkdGLLPLHI 343
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKS---GPLELAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 344 ASKKGNYrivqmllpvtsrTRvrrsGVSPLHLAAERNNDAVLEALLSARFDVNAP-------LAPERARLYEDRRSSALY 416
Cdd:TIGR00870 119 DQYTSEF------------TP----GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYHGESPLNAA 182
                         170       180
                  ....*....|....*....|..
gi 1622956763 417 FAVVNNNVYAteLLLEHGADPN 438
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADIL 202
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
593-632 3.28e-05

SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239696  Cd Length: 45  Bit Score: 41.37  E-value: 3.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
593-631 4.05e-05

SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239699  Cd Length: 42  Bit Score: 40.92  E-value: 4.05e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 631
Cdd:cd03729     3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
237-357 4.24e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 46.72  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAK---YGADINt 299
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPADIS- 171
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622956763 300 qASDSAS-----ALYEACKNEHE------EVVEFLLLQGADANK-------TNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22196   172 -ARDSMGntvlhALVEVADNTPEntkfvtKMYNEILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
593-631 4.53e-05

SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB5 has been implicated in the initiation of arteriogenesis. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239694  Cd Length: 42  Bit Score: 41.02  E-value: 4.53e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 631
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
290-344 5.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 5.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622956763 290 LAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIA 344
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
309-357 7.26e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 7.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622956763 309 YEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
PHA02798 PHA02798
ankyrin-like protein; Provisional
248-438 7.30e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 248 RND--LEVMEILVNGGAKVESKNAYGITPLF-----VAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEH---E 317
Cdd:PHA02798   46 RDSpsTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 318 EVVEFLLLQGADANKTNKDGLLPLHIASKKGNY---RIVQMLLP--VTSRTRVRRSGVSPLHLAAERNNDA----VLEAL 388
Cdd:PHA02798  126 EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgVDINTHNNKEKYDTLHCYFKYNIDRidadILKLF 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 389 LSARFDVNAPLAPERAR--------LYEDRRS----------------------SALYFAVVNNNVYATELLLEHGADPN 438
Cdd:PHA02798  206 VDNGFIINKENKSHKKKfmeylnslLYDNKRFkknildfifsyidinqvdelgfNPLYYSVSHNNRKIFEYLLQLGGDIN 285
PHA02859 PHA02859
ankyrin repeat protein; Provisional
264-381 9.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 264 VESKNAYGITPLF--VAAQSGQLEALRFLAKYGADINTQASDSA-SALYEAC---KNEHEEVVEFLLLQGADANKTNKDG 337
Cdd:PHA02859   44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622956763 338 LLPLHIASKKGNYRIVQMLLPVtsrtrvrRSGVSPLHLAAERNN 381
Cdd:PHA02859  124 KNLLHMYMCNFNVRINVIKLLI-------DSGVSFLNKDFDNNN 160
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
270-299 1.53e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.53e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622956763 270 YGITPLFVAAQSGQLEALRFLAKYGADINT 299
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
256-324 1.57e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622956763 256 ILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLL 324
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
270-298 1.75e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.75e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622956763  270 YGITPLFVAAQSGQLEALRFLAKYGADIN 298
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
593-633 3.59e-04

SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Asb4 was identified as imprinted gene in mice. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239693  Cd Length: 48  Bit Score: 38.58  E-value: 3.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622956763 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 633
Cdd:cd03723     3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
Ank_5 pfam13857
Ankyrin repeats (many copies);
224-275 3.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 3.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 224 LVQH-NADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPL 275
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02989 PHA02989
ankyrin repeat protein; Provisional
217-442 4.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.19  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 217 NAEAVKILVQHNADTNHRCN-RGWTALH---ESVSRNdLEVMEILVNGGAKV-ESKNAYGITPLFVAAQSG----QLEAL 287
Cdd:PHA02989  123 NCDMLRFLLSKGINVNDVKNsRGYNLLHmylESFSVK-KDVIKILLSFGVNLfEKTSLYGLTPMNIYLRNDidviSIKVI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 288 RFLAKYGADINTQasdsasalyeacKNEHEEVVEFLLlqgaDANKtnkdgllplhIASKKgNYRIVQMLLPVTSRTRVRR 367
Cdd:PHA02989  202 KYLIKKGVNIETN------------NNGSESVLESFL----DNNK----------ILSKK-EFKVLNFILKYIKINKKDK 254
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956763 368 SGVSPLHLAAERNNDAVLEALLSARFDVNAplaperarlYEDRRSSALYFAVVNNNVYATELLLehGADPNRDVI 442
Cdd:PHA02989  255 KGFNPLLISAKVDNYEAFNYLLKLGDDIYN---------VSKDGDTVLTYAIKHGNIDMLNRIL--QLKPGKYLI 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
410-501 6.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 6.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 410 RRSSALYFAVVNNNVYATELLLEHGADPNRDV-----ISPLLVAIRHGC---LRTMQLLLDHGANIDAYIATHPTAFPAT 481
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKYNLtdvKEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100
                  ....*....|....*....|
gi 1622956763 482 IMFAMKCLSLLKFLMDLGCD 501
Cdd:PHA03100  114 ISKKSNSYSIVEYLLDNGAN 133
Ank_4 pfam13637
Ankyrin repeats (many copies);
411-461 9.95e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 9.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 411 RSSALYFAVVNNNVYATELLLEHGADPNR---DVISPLLVAIRHGCLRTMQLLL 461
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
328-376 1.32e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622956763 328 ADANKTNKDGLLPLHIASKKGNYRIVQMLL-PVTSRTRVRRSGVSPLHLA 376
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLaYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
207-232 2.23e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.23e-03
                           10        20
                   ....*....|....*....|....*.
gi 1622956763  207 TPLYKACERKNAEAVKILVQHNADTN 232
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
369-397 2.25e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.25e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622956763  369 GVSPLHLAAERNNDAVLEALLSARFDVNA 397
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
186-303 2.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 186 DCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNrgwtalhesvsrndlevmeilvngg 261
Cdd:PHA02884   47 DIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAE------------------------- 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622956763 262 akvESKnaygITPLFVAAQSGQLEALRFLAKYGADINTQASD 303
Cdd:PHA02884  102 ---EAK----ITPLYISVLHGCLKCLEILLSYGADINIQTND 136
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
237-357 2.62e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 302
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQPaSLQAQ 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 303 DSAS-----ALYEACKN--EHEEVV----EFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22197   173 DSLGntvlhALVMIADNspENSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHIL 245
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
171-290 3.11e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 171 QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYKACERKNAEAVKILVQH---NADTNH 233
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENehqPADIEA 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 234 RCNRGWTALH-------ESVSRNDL--EVMEILVNGGAKV-------ESKNAYGITPLFVAAQSGQLEALRFL 290
Cdd:cd22193   155 QDSRGNTVLHalvtvadNTKENTKFvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYI 227
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
142-290 3.21e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 142 LHEAAYY---GQLGCLKVLQRAYPGTIDQRTL----------QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--- 205
Cdd:cd21882    30 LHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRffr 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 206 ----------ETPLYKACERKNAEAVKILVQHNADTNHRCNR---GWTALHESVSRND---------LEVMEILVNGGAK 263
Cdd:cd21882   110 kspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADntpensafvCQMYNLLLSYGAH 189
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622956763 264 V-------ESKNAYGITPLFVAAQSGQLEALRFL 290
Cdd:cd21882   190 LdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHI 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
108-227 4.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 108 PLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEA-AYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATcrGHLD 186
Cdd:PHA02878  204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSER 281
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622956763 187 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVKILVQH 227
Cdd:PHA02878  282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
PHA02736 PHA02736
Viral ankyrin protein; Provisional
285-365 5.19e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 285 EALRFLAKYGADINTQAS-DSASALYEACKNEHEEVVEFLLLQ-GADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR 362
Cdd:PHA02736   72 EKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151

                  ...
gi 1622956763 363 TRV 365
Cdd:PHA02736  152 CKV 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
237-265 5.30e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 5.30e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622956763  237 RGWTALHESVSRNDLEVMEILVNGGAKVE 265
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
303-450 5.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 5.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 303 DSASALYEACKNEHEEVVEFLLLQGADANKTNkdgllPLHIASKkgnyrivqmllpvtsrtrvrrsgVSPLHLAAERNND 382
Cdd:PHA02884   32 CIANILYSSIKFHYTDIIDAILKLGADPEAPF-----PLSENSK-----------------------TNPLIYAIDCDND 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622956763 383 AVLEALLSARFDVNaplaperaRLYEDRRSSALYFAVVNNNVYATELLLEHGADPN---RDVISPLLVAIR 450
Cdd:PHA02884   84 DAAKLLIRYGADVN--------RYAEEAKITPLYISVLHGCLKCLEILLSYGADINiqtNDMVTPIELALM 146
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
596-631 5.61e-03

SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2), and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh), as well as, their isoforms WSB-2 and SWiP-2. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239702  Cd Length: 39  Bit Score: 35.09  E-value: 5.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622956763 596 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 631
Cdd:cd03733     6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
237-357 5.95e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 39.83  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 237 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYG---ADINT 299
Cdd:cd22195   136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQPDIVHYLTENAhkkADLRR 215
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956763 300 QASDSAS---ALYEACKNEHE------EVVEFLLLQGA----DANKT---NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22195   216 QDSRGNTvlhALVAIADNTREntkfvtKMYDLLLIKCAklypDCNLEailNNDGMSPLMMAAKLGKIGIFQHII 289
PHA02792 PHA02792
ankyrin-like protein; Provisional
250-337 6.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 39.55  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 250 DLEVME-ILVNGGAKVES-KNAYGITPLFVAAQSGQLEALRFLA---KYGADINTQASDSASALYEACKNEHEEVVEFLL 324
Cdd:PHA02792  351 DPKVVEyILKNGNVVVEDdDNIINIMPLFPTLSIHESDVLSILKlckPYIDDINKIDKHGRSILYYCIESHSVSLVEWLI 430
                          90
                  ....*....|...
gi 1622956763 325 LQGADANKTNKDG 337
Cdd:PHA02792  431 DNGADINITTKYG 443
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
596-633 7.72e-03

SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ABS3 has been shown to be negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of tumor necrosis factor receptor II (TNF-R2) for ubiquitination and proteasome-mediated degradation. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239692  Cd Length: 51  Bit Score: 34.77  E-value: 7.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622956763 596 LAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYEN 633
Cdd:cd03722     6 LTHLCRLEIRSSLKSERLRsdsFICQLPLPRSLQDYLLYSD 46
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
185-275 7.84e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.51  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 185 LDCLLSLLQAGAEPDISNKSRETPLYKACERKN--AEAVKILVQHNADTNHRCNRGWTALHESVSR------------ND 250
Cdd:PHA02716  297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdND 376
                          90       100
                  ....*....|....*....|....*..
gi 1622956763 251 --LEVMEILVNGGAKVESKNAYGITPL 275
Cdd:PHA02716  377 irLDVIQCLISLGADITAVNCLGYTPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
443-469 8.66e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.66e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622956763  443 SPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
374-463 9.48e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 9.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763 374 HLAAerNNDAV-LEALLSARFDVNAplaperaRLYEDRrsSALYFAVVNNNVYATELLLEHGADP---NRDVISPLLVAI 449
Cdd:PTZ00322   88 QLAA--SGDAVgARILLTGGADPNC-------RDYDGR--TPLHIACANGHVQVVRVLLEFGADPtllDKDGKTPLELAE 156
                          90
                  ....*....|....
gi 1622956763 450 RHGCLRTMQLLLDH 463
Cdd:PTZ00322  157 ENGFREVVQLLSRH 170
PHA02884 PHA02884
ankyrin repeat protein; Provisional
98-227 9.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 9.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956763  98 FQTSQLAPVDPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWL-PLHEAAYYGQLGCLKVLQRAYPgTIDQRTLQEETAV 176
Cdd:PHA02884   63 FPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKItPLYISVLHGCLKCLEILLSYGA-DINIQTNDMVTPI 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622956763 177 YLAT--CRGHldclLSLLQAGAEPDISNKSRETPLYkacerkNAEAVKILVQH 227
Cdd:PHA02884  142 ELALmiCNNF----LAFMICDNEISNFYKHPKKILI------NFDILKILVSH 184
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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